Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1F28

CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII BOUND TO DUMP AND BW1843U89

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004799	molecular_function	thymidylate synthase activity
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006231	biological_process	dTMP biosynthetic process
A	0006235	biological_process	dTTP biosynthetic process
A	0008168	molecular_function	methyltransferase activity
A	0009165	biological_process	nucleotide biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016741	molecular_function	transferase activity, transferring one-carbon groups
A	0032259	biological_process	methylation
B	0004799	molecular_function	thymidylate synthase activity
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006231	biological_process	dTMP biosynthetic process
B	0006235	biological_process	dTTP biosynthetic process
B	0008168	molecular_function	methyltransferase activity
B	0009165	biological_process	nucleotide biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016741	molecular_function	transferase activity, transferring one-carbon groups
B	0032259	biological_process	methylation
C	0004799	molecular_function	thymidylate synthase activity
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006231	biological_process	dTMP biosynthetic process
C	0006235	biological_process	dTTP biosynthetic process
C	0008168	molecular_function	methyltransferase activity
C	0009165	biological_process	nucleotide biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016741	molecular_function	transferase activity, transferring one-carbon groups
C	0032259	biological_process	methylation
D	0004799	molecular_function	thymidylate synthase activity
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006231	biological_process	dTMP biosynthetic process
D	0006235	biological_process	dTTP biosynthetic process
D	0008168	molecular_function	methyltransferase activity
D	0009165	biological_process	nucleotide biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016741	molecular_function	transferase activity, transferring one-carbon groups
D	0032259	biological_process	methylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE UMP A 301

Chain	Residue
A	ARG26
A	ASN210
A	HIS240
A	TYR242
A	F89401
A	HOH519
B	ARG153
B	ARG154
B	HOH741
A	LEU170
A	CYS173
A	HIS174
A	GLN198
A	ARG199
A	SER200
A	ASP202
A	GLY206

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UMP B 302

Chain	Residue
A	ARG153
A	ARG154
B	ARG26
B	LEU170
B	CYS173
B	HIS174
B	GLN198
B	ARG199
B	SER200
B	ASP202
B	ASN210
B	HIS240
B	TYR242
B	F89402
B	HOH682
B	HOH748

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE UMP C 303

Chain	Residue
C	ARG26
C	TYR113
C	LEU170
C	CYS173
C	HIS174
C	GLN198
C	ARG199
C	SER200
C	ASP202
C	GLY206
C	ASN210
C	HIS240
C	TYR242
C	F89403
C	HOH589
D	ARG153
D	ARG154

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UMP D 304

Chain	Residue
C	ARG153
C	ARG154
C	HOH756
D	ARG26
D	LEU170
D	CYS173
D	HIS174
D	GLN198
D	ARG199
D	SER200
D	ASP202
D	ASN210
D	HIS240
D	TYR242
D	F89404
D	HOH690

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE F89 A 401

Chain	Residue
A	PHE58
A	GLY61
A	GLU65
A	HIS85
A	ILE86
A	TRP87
A	ASN90
A	LEU170
A	ASP202
A	LEU205
A	GLY206
A	PHE209
A	SER296
A	UMP301

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE F89 B 402

Chain	Residue
B	PHE58
B	GLY61
B	GLU65
B	HIS85
B	ILE86
B	TRP87
B	ASN90
B	ASP202
B	GLY206
B	PHE209
B	TYR242
B	MET295
B	ILE297
B	UMP302
B	HOH643

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE F89 C 403

Chain	Residue
C	ILE86
C	TRP87
C	ASN90
C	LEU170
C	ASP202
C	LEU205
C	GLY206
C	PHE209
C	TYR242
C	SER296
C	UMP303
C	PHE58
C	GLY61
C	GLU65
C	HIS85

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE F89 D 404

Chain	Residue
D	PHE58
D	GLY61
D	GLU65
D	HIS85
D	ILE86
D	TRP87
D	ASN90
D	ASP202
D	GLY206
D	PHE209
D	TYR242
D	MET295
D	ILE297
D	UMP304

Functional Information from PROSITE/UniProt

site_id	PS00091
Number of Residues	29
Details	THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrlIlsaWNpadlekma.....LpPCHmfcQFyV

Chain	Residue	Details
A	ARG153-VAL181

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	28
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A884","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1lcb

Chain	Residue	Details
A	SER200
A	ASP238
A	GLU65
A	CYS173
A	HIS240
A	ASP202

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1lcb

Chain	Residue	Details
B	SER200
B	ASP238
B	GLU65
B	CYS173
B	HIS240
B	ASP202

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1lcb

Chain	Residue	Details
C	SER200
C	ASP238
C	GLU65
C	CYS173
C	HIS240
C	ASP202

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1lcb

Chain	Residue	Details
D	SER200
D	ASP238
D	GLU65
D	CYS173
D	HIS240
D	ASP202

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)